Journal article
Diversity in the protein N-glycosylation pathways within the Campylobacter genus
H Nothaft, NE Scott, E Vinogradov, X Liu, R Hu, B Beadle, C Fodor, WG Miller, J Li, SJ Cordwell, CM Szymanski
Molecular and Cellular Proteomics | ELSEVIER | Published : 2012
Open access
Abstract
The foodborne bacterial pathogen, Campylobacter jejuni, possesses an N-linked protein glycosylation (pgl) pathway involved in adding conserved heptasaccharides to aspar-agine- containing motifs of >60 proteins, and releasing the same glycan into its periplasm as free oligosaccharides. In this study, comparative genomics of all 30 fully sequenced Campylobacter taxa revealed conserved pgl gene clusters in all but one species. Structural, phylogenetic and immunological studies showed that the N-glycosylation systems can be divided into two major groups. Group I includes all thermotolerant taxa, capable of growth at the higher body temperatures of birds, and produce the C. jejuni-like glycans. W..
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Awarded by Medical Research Foundation
Funding Acknowledgements
This work was supported by the Alberta Glycomics Centre. NES holds a CJ Martin Overseas Biomedical Postdoctoral Research Fellowship from the Australian National Health and Medical Research Foundation (#APP1037373). CMS holds an Alberta Innovates Scholar award.